1x75: Difference between revisions

Revision as of 13:37, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1x75.png

Template:STRUCTURE 1x75

CcdB:GyrA14 complexCcdB:GyrA14 complex

Template:ABSTRACT PUBMED 15854646

About this StructureAbout this Structure

1X75 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of gyrase poisoning by the addiction toxin CcdB., Dao-Thi MH, Van Melderen L, De Genst E, Afif H, Buts L, Wyns L, Loris R, J Mol Biol. 2005 May 20;348(5):1091-102. Epub 2005 Apr 7. PMID:15854646

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OCA

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-'''CcdB:GyrA14 complex'''
+===CcdB:GyrA14 complex===
-==Overview==
+<!--
-Gyrase is an ubiquitous bacterial enzyme that is responsible for disentangling DNA during DNA replication and transcription. It is the target of the toxin CcdB, a paradigm for plasmid addiction systems and related bacterial toxin-antitoxin systems. The crystal structure of CcdB and the dimerization domain of the A subunit of gyrase (GyrA14) dictates an open conformation for the catalytic domain of gyrase when CcdB is bound. The action of CcdB is one of a wedge that stabilizes a dead-end covalent gyrase:DNA adduct. Although CcdB and GyrA14 form a globally symmetric complex where the two 2-fold axes of both dimers align, the complex is asymmetric in its details. At the centre of the interaction site, the Trp99 pair of CcdB stacks with the Arg462 pair of GyrA14, explaining why the Arg462Cys mutation in the A subunit of gyrase confers resistance to CcdB. Overexpression of GyrA14 protects Escherichia coli cells against CcdB, mimicking the action of the antidote CcdA.
+The line below this paragraph, {{ABSTRACT_PUBMED_15854646}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15854646 is the PubMed ID number.
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 [[Category: Ta system]]
 [[Category: Topoisomerase]]
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